The similarity of the glyceraldehyde-3-phosphate dehydrogenases isolated from rabbit brain and muscle

Kochman, Marian; Rutter, William J.

doi:10.1021/bi00845a008

Cited by 27 publications

(4 citation statements)

References 41 publications

(29 reference statements)

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“…Dr. Marian Kochman of this Department (Kochman and Rutter, 1968). The sedimented crystals were dissolved in buffer to a concentration of about 30 g/1.…”

Section: Methodsmentioning

confidence: 95%

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Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Hoagland¹,

Teller²

1969

Biochemistry

160

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A preparation of rabbit muscle D-glyCeraldehyde 3-phosphate dehydrogenase which dissociates reversibly at neutral pH has been studied. The system can be described by a dimer-tetramer reversible equilibrium with association constant of 2 X IO8 l./mole at pH 7 and low ionic strength at 5 ', When added together, diphosphopyridine nucleotide and phosphate shift the equilibrium toward tetramer (kz = 5 X lo6 I./mole). Either substrate alone does not produce an effect. Acylation of the enzyme by the combination of glyceraldehyde, phosphate, and diphosphopyridine nucleotide produces an irreversible dissociation to dimer. It is concluded that the dissociated species is the 6-aminoacyl enzyme of Mathew et al. (Mathew, E., Meriwether, B. P., and Park, J. H. (1967), J . Biol. Chem. 242,5024). p-Nitrophenyl acetive enzyme sedimentation studies (t a i -1 ER Lyulllurlulll. A C -T he molecular weight of mammalian muscle D-glyCeraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) has been investigated in several laboratories. Molecular weight determinations by sedimentation velocity and diffusion yielded values of approximately 120 x lo3 (Taylor et al., 1956;Elias et al., 1960) and 143 X lo3 g/mole (Elodi, 1958). Dandliker and Fox (1955) and Fox andDandliker (1956a,b)found 140 x lo3 by light scattering and 137 x lo3 g/mole by sedimentation velocity and diffusion. Using the Archibald method, Elias et al. (1960) found a molecular weight of 118 X lo3. More recently Harrington and Karr (1965) have observed 145 X lo3 g/mole using both sedimentation velocity and sedimentation equilibrium. Jaenicke et al. (1968) have found the same value for the native enzyme and have also concluded that the tetramer does not dissociate in solution except at extremes of pH, ionic strength, and in the presence of detergents.Harris and Perham (1965) have reported that glyceraldehyde 3-phosphate dehydrogenase is composed of four identical subunits. Harrington and Karr (1965) have shown that the enzyme is dissociated to a monomer of 36.3 X lo3 g/mole in 5 M guanidine hydrochloride. The dissociation reported by Jaenicke et al. (1968) was also found to proceed to themonomer stage. Elodi (1958) claimed that KCN produced a halving of the molecular Medical Sciences (l-F2-GM-37.340-01). Conipt. Rend. 260,2077) have been performed to determine the size of the catalytic unit. As a dehydrogenase, only the tetrameric form of the enzyme is active. Esterase activity is present in the dimer and apparently also in the tetrameric state of association. Studies with the apoenzyme both by short-column sedimentation equilibrium and by sedimentation velocity indicates that the preparation initially consists of both dimer and tetramer. After longer periods, the enzyme further dissociates to monomer as well as aggregates to a high degree, Finally, a computation procedure has been developed for the determination of equilibrium constants for highly associated systems of dimers and tetramers (or monomers and dimers). In addition a method of accurately calculating the molecular weigh...

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“…Dr. Marian Kochman of this Department (Kochman and Rutter, 1968). The sedimented crystals were dissolved in buffer to a concentration of about 30 g/1.…”

Section: Methodsmentioning

confidence: 95%

“…Crystalline rabbit muscle glyceraldehyde 3-phosphate dehydrogenase was prepared and generously donated by Dr. Marian Kochman of this Department (Kochman and Rutter, 1968). The sedimented crystals were dissolved in buffer to a concentration of about 30 g/l.…”

Section: Methodsmentioning

confidence: 99%

Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Hoagland¹,

Teller²

1969

Biochemistry

160

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“…Tryptic Peptide Analysis. Method I. Tryptic peptides of in vitro synthesized proteins were prepared according to the procedure of Kochman and Rutter (1968) with the following modifications: 5 mL of the in vitro translation mixture was adjusted to 10 mM EDTA (pH 7.4) and incubated with 0.5 Mg of pancreatic ribonuclease for 30 min at 37 °C. After ribonuclease treatment, the sample was dissolved in 1 mL of 8 M urea in 0.1 M ammonium bicarbonate (pH 8.2) and 10 mM dithiothreitol, and 50 Mg of the appropriate purified glycolytic enzyme was added.…”

Section: Methodsmentioning

confidence: 99%

Isolation and identification of yeast messenger ribonucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate kinase

Holland¹,

Holland²

1978

Biochemistry

145

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Yeast poly(adenylic acid)-containing messenger ribonucleic acid isolated from two strains of Saccharomyces cerevisiae was fractionated by preparative polyacrylamide gel electrophoresis in the presence of formamide. Three messenger ribonucleic acids, present at high intracellular concentration, were electrophoretically eluted from the polyacrylamide gels and translated in a wheat germ cell-free extract. The in vitro synthesized polypeptides were identified by tryptic peptide analysis. Messenger ribonucleic acids coding for enolase and glyceraldehyde-3-phosphate dehydrogenase were isolated from commercially grown baker's yeast (strain F1), and messenger ribonucleic acid coding for phosphoglycerate kinase was isolated from Saccharomyces cerevisiae (ATCC 24657). Significant differences in the spectrum of abundant messenger ribonucleic acids isolated from commercially grown baker's yeast (strain F1) and strain 24657 were observed. When both strains were grown under identical conditions, however, the spectrum of messenger ribonucleic acid isolated from the cells is indistinguishable.

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“…Glyceraldehyde-3-phosphate dehydrogenase was prepared from rabbit muscle according to Kochman and Rutter [16]. Phosphatidylinositol from bovine brain, o-phthaldialdehyde and 2-mercaptoethanol were purchased from Koch-Light Laboratories, Sigma and Fluka, respectively.…”

Section: Methodsmentioning

confidence: 99%

Fluorescent probe studies on binding of glyceraldehyde‐3‐phosphate dehydrogenase to phosphatidylinositol liposomes Further evidence for conformational changes

Michalak¹,

Gutowicz²,

Modrzycka³

1987

FEBS Letters

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Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle can be adsorbed on charged lipid bilayers by electrostatic forces. Upon binding to phosphatidylinositol liposomes the enzyme modifies its conformational state as it is shown by resonance energy transfer experiments. In the presence of 2-mercaptoethanol o-phthaldialdehyde reacts with amino groups of the protein and the covalently bound fluorophore is an acceptor of excitation energy transferred from tryptophanyl residues of the protein. The observed decrease of energy transfer efficiency upon binding to phosphatidylinositol liposomes is compared with the influence of the urea on the fluorescence spectra of the labelled protein. Significance of conformational changes of the enzyme upon adsorption on liposomes in the regulating function of cell membranes is discussed.

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The similarity of the glyceraldehyde-3-phosphate dehydrogenases isolated from rabbit brain and muscle

Cited by 27 publications

References 41 publications

Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Isolation and identification of yeast messenger ribonucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate kinase

Fluorescent probe studies on binding of glyceraldehyde‐3‐phosphate dehydrogenase to phosphatidylinositol liposomes Further evidence for conformational changes

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